dc.contributor.author | Bowen, Hannah G. | |
dc.contributor.author | Kenedy, Melisha R. | |
dc.contributor.author | Johnson, David K. | |
dc.contributor.author | MacKerell, Alexander D., Jr. | |
dc.contributor.author | Akins, Darrin R. | |
dc.date.accessioned | 2023-08-16T14:40:05Z | |
dc.date.available | 2023-08-16T14:40:05Z | |
dc.date.issued | 2023-06-29 | |
dc.identifier.citation | Hannah G Bowen and others, Identification of a novel transport system in Borrelia burgdorferi that links the inner and outer membranes, Pathogens and Disease, Volume 81, 2023, ftad014, https://doi.org/10.1093/femspd/ftad014 | en_US |
dc.identifier.uri | https://hdl.handle.net/1808/34737 | |
dc.description.abstract | Borrelia burgdorferi, the spirochete that causes Lyme disease, is a diderm organism that is similar to Gram-negative organisms in that it contains both an inner and outer membrane. Unlike typical Gram-negative organisms, however, B. burgdorferi lacks lipopolysaccharide (LPS). Using computational genome analyses and structural modeling, we identified a transport system containing six proteins in B. burgdorferi that are all orthologs to proteins found in the lipopolysaccharide transport (LPT) system that links the inner and outer membranes of Gram-negative organisms and is responsible for placing LPS on the surface of these organisms. While B. burgdorferi does not contain LPS, it does encode over 100 different surface-exposed lipoproteins and several major glycolipids, which like LPS are also highly amphiphilic molecules, though no system to transport these molecules to the borrelial surface is known. Accordingly, experiments supplemented by molecular modeling were undertaken to determine whether the orthologous LPT system identified in B. burgdorferi could transport lipoproteins and/or glycolipids to the borrelial outer membrane. Our combined observations strongly suggest that the LPT transport system does not transport lipoproteins to the surface. Molecular dynamic modeling, however, suggests that the borrelial LPT system could transport borrelial glycolipids to the outer membrane. | en_US |
dc.publisher | Pathogens and Disease | en_US |
dc.rights | Copyright © 2023, Oxford University Press. This is an open access article distributed under the terms of the Creative Commons CC BY license. | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | en_US |
dc.subject | Lipopolysaccharide transport (LPT) | en_US |
dc.subject | Glycolipids | en_US |
dc.subject | Lipoproteins | en_US |
dc.subject | Borrelia burgdorferi | en_US |
dc.subject | Site Identification by Ligand Competitive Saturation (SILCS) | en_US |
dc.title | Identification of a novel transport system in Borrelia burgdorferi that links the inner and outer membranes | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Johnson, David K. | |
kusw.kudepartment | Shenkel Structural Biology Center | en_US |
kusw.kudepartment | Molecular Graphics and Modeling Laboratory | en_US |
kusw.kudepartment | Computational Biology Core | en_US |
dc.identifier.doi | 10.1093/femspd/ftad014 | en_US |
dc.identifier.orcid | https://orcid.org/0009-0008-3712-664X | en_US |
kusw.oaversion | Scholarly/refereed, publisher version | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC10353723 | en_US |
dc.rights.accessrights | openAccess | en_US |